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Interleukin 17A (IL17A) (Active) Protein

Details for Product No. ABIN413453
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Protein Name
Synonyms Il17, IL17A, CTLA8, IL-17, IL-17A, IL17, Ctla-8, Ctla8, CTLA-8, ChIL-17, IL-17F
(56), (31), (27), (3), (2), (1), (1), (1)
Escherichia coli (E. coli)
(93), (4), (2), (1)
Protein Type Recombinant
Biological Activity Active
Western Blotting (WB), ELISA, Functional Studies (Func)
Pubmed 2 references available
Quantity 1 mg
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Catalog No. ABIN413453
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Characteristics Biological activity: less than 2 ng/mL The ED50 as determined by the dose-dependent induction of IL-6 in primary human foreskin fibroblasts is less than 2 ng/mL, corresponding to a specific activity of more than 5 x 10^5 U/mg.
Purity > 98 % by SDS-PAGE and HPLC analysis
Sterility Sterile filtered
Endotoxin Level < 0.1 ng/μg
Alternative Name IL-17A
Background The original described IL-17 protein, now known as IL-17A, was identified from a CD4+ T cells DNA library. IL-17 can be induced from primary peripheral blood CD4+ T cells upon stimulation. Supernatant from cells transfected with IL-17 induced IL-16 and IL-18 production and enhanced the surface expression of the intraCellular adhesion molecule-1 (ICAM-1) in human fibroblasts. Recombinant IL-17 is a 31 kDa disulfide-linked homodier of two 136 amino acid polypeptide chains.
Synonyms: Human IL-17A, IL-17A, IL17A, IL 17 A, h-IL-17A, rh-IL-17A, recombinant human IL-17A, recombinant IL-17, IL, interluekin, IL17A/F, IL17 A/F, IL-17A/F Interleukin-17 A/F, Interleukin-17 AF
Molecular Weight 31.0 kDa
Gene ID 3605
UniProt Q16552
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in H2O to a concentration of 0.1-1.0 mg/mL. The solution can then be diluted into other aqueous buffers and stored at 4 °C for 1 week or -20 °C for future use.
Buffer Lyophilized with no additives
Preservative Without preservative
Handling Advice Centrifuge the vial prior to opening.
Storage -20 °C
Expiry Date 12 months
Product cited in: Roussel, Houle, Chan et al.: "IL-17 promotes p38 MAPK-dependent endothelial activation enhancing neutrophil recruitment to sites of inflammation." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 184, Issue 8, pp. 4531-7, 2010 (PubMed).

Bérubé, Roussel, Nattagh et al.: "Loss of cystic fibrosis transmembrane conductance regulator function enhances activation of p38 and ERK MAPKs, increasing interleukin-6 synthesis in airway epithelial cells exposed to Pseudomonas aeruginosa." in: The Journal of biological chemistry, Vol. 285, Issue 29, pp. 22299-307, 2010 (PubMed).

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